Cooperative binding of midazolam with testosterone and alpha-naphthoflavone within the CYP3A4 active site: a NMR T1 paramagnetic relaxation study.

@article{Cameron2005CooperativeBO,
  title={Cooperative binding of midazolam with testosterone and alpha-naphthoflavone within the CYP3A4 active site: a NMR T1 paramagnetic relaxation study.},
  author={Michael D. Cameron and Bo Wen and Kyle E Allen and Arthur G. Roberts and Jason T. Schuman and Alexander P. Campbell and Kent L. Kunze and Sidney D. Nelson},
  journal={Biochemistry},
  year={2005},
  volume={44 43},
  pages={
          14143-51
        }
}
Recent studies have indicated that CYP3A4 exhibits non-Michaelis-Menten kinetics for numerous substrates. Both homo- and heterotropic activation have been reported, and kinetic models have suggested multiple substrates within the active site. We provide some of the first physicochemical data supporting the hypothesis of allosteric substrate binding within the CYP3A4 active site. Midazolam (MDZ) is metabolized by CYP3A4 to two hydroxylated metabolites, 1'- and 4-hydroxymidazolam. Incubations… CONTINUE READING
Highly Cited
This paper has 25 citations. REVIEW CITATIONS

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 11 citations